APP, 18-289aa, Human

Category: Proteins
Catalog
01-P1499
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Product Name APP, 18-289aa, Human
Description APP, also known as amyloid beta A4 protein, functions as a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Recombinant human APP protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.
Synonyms Amyloid beta A4 protein, AAA, AD1, PN2, ABPP, APPI, CVAP, ABETA, CTFgamma
Host E. coli
Molecular Weight 39.8 kDa (347aa) confirmed by MALDI-TOF
Amino Acid Sequence MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSLEVP TDGNAGLLAE PQIAMFCGRL NMHMNVQNGK WDSDPSGTKT CIDTKEGILQ YCQEVYPELQ ITNVVEANQP VTIQNWCKRG RKQCKTHPHF VIPYRCLVGE FVSDALLVPD KCKFLHQERM DVCETHLHWH TVAKETCSEK STNLHDYGML LPCGIDKFRG VEFVCCPLAE ESDNVDSADA EEDDSDVWWG GADTDYADGS EDKVVEVAEE EEVAEVEEEE ADDDEDDEDG DEVEEEAEEP YEEATERTTS IATTTTTTTE SVEEVVRE
Tag His-tag
Reactivity Human
Applications SDS-PAGE
Form Liquid, in 20mM Tris-HCl buffer (pH8.0) containing 30% glycerol, 0.15M NaCl, 1mM DTT
Concentration 1mg/ml (determined by Bradford assay)
Purity > 85% by SDS-PAGE
Storage Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles.
References Kontush A., et al. (2001) Cell. Mol. Neurobiol. 21:299-315 Walter M.F., et al. (2006) Biochem. Biophys. Res. Commun. 233:760-764
Background APP, also known as amyloid beta A4 protein, functions as a cell surface receptor and transmembrane precursor protein that is cleaved by secretases to form a number of peptides. Some of these peptides are secreted and can bind to the acetyltransferase complex APBB1/TIP60 to promote transcriptional activation, while others form the protein basis of the amyloid plaques found in the brains of patients with Alzheimer disease. Mutations in this gene have been implicated in autosomal dominant Alzheimer disease and cerebroarterial amyloidosis (cerebral amyloid angiopathy). Recombinant human APP protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography.
Supplier ARP

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